scholarly journals Cloning and analysis of monkey fertilin reveals novel α subunit isoforms

1995 ◽  
Vol 307 (3) ◽  
pp. 843-850 ◽  
Author(s):  
A C F Perry ◽  
P M Gichuhi ◽  
R Jones ◽  
L Hall
Keyword(s):  
Macaca Fascicularis ◽  
Surface Membrane ◽  
Beta Subunits ◽  
Cdna Clones ◽  
Head Region ◽  
Α Subunit ◽  
Pcr Products ◽  
Testis Cdna ◽  
High Level ◽  
Mammalian Spermatozoa

The fertilin complex, a heterodimeric surface membrane glycoprotein found on the head region of mammalian spermatozoa, has been reported to mediate membrane fusion with the egg plasma membrane during fertilization. We have employed PCR to generate products corresponding to monkey (Macaca fascicularis) fertilins from testis cDNA. These PCR products have been used to isolate full-length fertilin cDNA clones corresponding to both alpha and beta subunits. Both monkey fertilin alpha and beta cDNAs encode proteins which belong to an expanding family of metalloproteinase-like, disintegrin-like, cysteine-rich, mammalian proteins. Surprisingly, cDNAs for two fertilin alpha isoforms, alpha I and alpha II, were isolated, encoding proteins of 905 and 825 residues respectively. The predicted fertilin alpha isoforms share extensive identity, but differ significantly towards their N- and C-termini, suggesting the possibility of more than one type of fertilin complex in primates. Alignment of monkey alpha and beta fertilins with their respective guinea-pig counterparts suggests a high level of overall structural conservation throughout, whilst providing new insights into the domain function of each.

scholarly journals The human fertilin α gene is non-functional: implications for its proposed role in fertilization

1997 ◽  
Vol 321 (3) ◽  
pp. 577-581 ◽  
Author(s):  
Jennifer A. JURY ◽  
Jan FRAYNE ◽  
Len HALL
Keyword(s):  
Plasma Membrane ◽  
Guinea Pig ◽  
Genetic Recombination ◽  
Surface Membrane ◽  
Membrane Glycoprotein ◽  
Head Region ◽  
Α Subunit ◽  
Functional Implications ◽  
Mammalian Fertilization

In the guinea-pig, the α subunit of the fertilin complex, a heterodimeric surface membrane glycoprotein found on the head region of spermatozoa, has previously been proposed to mediate membrane fusion with the oolemma plasma membrane during fertilization. Here we describe experiments which indicate that the only fertilin α-like gene in humans is an expressed, but non-functional, pseudogene, possibly derived by genetic recombination between the two fertilin α genes found in some primates. This finding clearly raises questions about the importance and/or role of fertilin α in mammalian fertilization.

scholarly journals Evaluation of nutritional values of smoke cured riverine and marine hilsa (Tenualosa ilisha; Hamilton, 1882)

2018 ◽  
Vol 46 (2) ◽  
pp. 177-184
Author(s):  
Sumon Debnath ◽  
Gulshan Ara Latifa ◽  
Mohajira Begum ◽  
Md Abu Obaida
Keyword(s):  
Head Region ◽  
Nutritional Values ◽  
Caudal Region ◽  
Abdominal Region ◽  
Before And After ◽  
Tenualosa Ilisha ◽  
High Level

Present study was conducted to evaluate nutritional values of smoked hilsa fish (Tenualosa ilisha; Hamilton, 1882) in relation to its raw condition. Smoking is one of the processes of fish preservation from ancient period of our country. The nutrients values of the hilsa from two different regions were significantly (p < 0.05) varied. The nutritional values were different before and after processing of hilsa. Riverine hilsa contains relatively more moisture (56.45 ± 0.51%) and protein (15.98 ± 0.50%) than marine hilsa. Fat (16.18 ± 0.45%) and salt (1.92 ± 0.18%) contents are higher in marine hilsa; whereas ash (8.34 ± 0.35%) content was higher in riverine hilsa. Minerals like iron (4.72 ± 0.08 mg/100 g) and calcium (481.77 ± 6.20 mg/100g) remain in large amount on marine hilsa but phosphorus (115.73 ± 4.36 mg/100 g) content remain high level in riverine hilsa. In addition, the protein (raw condition, 19.54 ± 0.47%, riverine; 17.12 ± 0.42%, marine and smoked condition, 29.64 ± 0.41%, riverine; 28.51 ± 0.51%, marine) and fat (raw condition, 16.41 ± 0.46%, riverine; 20.07 ± 0.39%, marine and smoked condition, 20.71 ± 0.47%, riverine; 23.31 ± 0.47%, marine) content were higher in abdominal region of riverine and marine hilsa both raw and smoked condition than head region (protein in raw condition, 11.21 ± 0.51%, riverine; 10.51 ± 0.53%, marine and smoked condition, 17.14 ± 0.42%, riverine; 15.69 ± 0.4%, marine; fat in raw condition, 9.04 ± 0.45%, riverine; 11.21 ± 0.51%, marine and smoked condition, 12.32 ± 0.44%, riverine; 14.56 ± 0.47%, marine) and caudal region (protein in raw condition17.21 ± 0.52%, riverine; 15.22 ± 0.66%, marine and smoked condition, 27.68 ± 0.44%, riverine; 26.73 ± 0.46%, marine; fat in raw condition, 14.05 ± 0.5%, riverine; 17.28 ± 0.47%, marine and smoked condition, 17.35 ± 0.43%, riverine; 19.18 ± 0.51%, marine). Bangladesh J. Zool. 46(2): 177-184, 2018

Testis-specific transcription initiation sites of rat farnesyl pyrophosphate synthetase mRNA

1990 ◽  
Vol 10 (5) ◽  
pp. 2315-2326
Author(s):  
J H Teruya ◽  
S Y Kutsunai ◽  
D H Spear ◽  
P A Edwards ◽  
C F Clarke
Keyword(s):  
Transcription Initiation ◽  
Untranslated Region ◽  
In Vitro Translation ◽  
Cdna Clones ◽  
Rat Tissues ◽  
Farnesyl Pyrophosphate ◽  
S1 Nuclease ◽  
Testis Cdna ◽  
Low Efficiency

A variety of rat tissues were screened at low stringency with a rat farnesyl pyrophosphate (FPP) synthetase cDNA. In testis, an FPP synthetase-related RNA was detected that was larger than the liver FPP synthetase mRNA and was present at very high levels comparable with liver FPP synthetase RNA levels obtained from rats fed diets supplemented with cholestyramine and mevinolin. Sequence analysis of testis cDNA clones, together with primer extension and S1 nuclease experiments, indicated that testis FPP synthetase transcripts contain an extended 5' untranslated region. The 5' extension contained one or two out-of-frame upstream ATGs, depending on the site of transcription initiation. Protein in vitro translation studies indicated that the extended 5' untranslated region may play a role in regulating the translation of the FPP synthetase polypeptide in rat testis. Southern blot analysis with a probe containing both testis and liver 5' untranslated sequences provided evidence that both liver and testis transcripts derive from the same gene. The data suggest that an upstream testis-specific promoter results in the abundant production of FPP synthetase transcripts that are translated at low efficiency; another promoter functions in liver and other somatic tissues and directs the regulated synthesis of shorter discrete transcripts.

Interaction of the α subunit of Na,K-ATPase with cofilin

2001 ◽  
Vol 353 (2) ◽  
pp. 377-385 ◽  
Author(s):  
Kyunglim LEE ◽  
Jaehoon JUNG ◽  
Miyoung KIM ◽  
Guido GUIDOTTI
Keyword(s):  
Actin Binding ◽  
Cdna Clones ◽  
Cytoplasmic Loop ◽  
Α Subunit ◽  
Transmembrane Segments ◽  
Yeast Two Hybrid System ◽  
Membrane Bound ◽  
Two Hybrid ◽  
Α1 Subunit

The α1 subunit of rat Na,K-ATPase, composed of 1018 amino acids, is arranged in the membrane so that the middle third of the polypeptide forms a large cytoplasmic loop bordered on both sides by multiple transmembrane segments. To identify proteins that might interact with the large cytoplasmic loop of Na,K-ATPase and potentially affect the function and/or the disposition of the pump in the cell, the yeast two-hybrid system was used to screen a rat skeletal muscle cDNA library. Several cDNA clones were isolated, some of which coded for cofilin, an actin-binding protein. Cofilin was co-immunoprecipitated with the α subunit of Na,K-ATPase from extracts of COS-7 cells transiently transfected with haemagglutinin-epitope-tagged cofilin cDNA as well as from yeast extracts. By means of deletion analysis we showed that the segment of cofilin between residues 45 and 99 is essential for functional association with the large cytoplasmic loop of Na,K-ATPase. Recombinant cofilin was shown to bind to the membrane-bound Na,K-ATPase; the association between the two proteins was demonstrated by confocal microscopy. The increased level of cofilin in transfected COS-7 cells caused an increase in the rate of ouabain-sensitive 86Rb+ uptake, indicating that cofilin elicits, either directly or indirectly, enhanced Na,K-ATPase activity and that the interaction occurs in vivo.

scholarly journals Testis-specific transcription initiation sites of rat farnesyl pyrophosphate synthetase mRNA.

1990 ◽  
Vol 10 (5) ◽  
pp. 2315-2326 ◽  
Author(s):  
J H Teruya ◽  
S Y Kutsunai ◽  
D H Spear ◽  
P A Edwards ◽  
C F Clarke
Keyword(s):  
Transcription Initiation ◽  
Untranslated Region ◽  
In Vitro Translation ◽  
Cdna Clones ◽  
Rat Tissues ◽  
Farnesyl Pyrophosphate ◽  
S1 Nuclease ◽  
Testis Cdna ◽  
Low Efficiency

A variety of rat tissues were screened at low stringency with a rat farnesyl pyrophosphate (FPP) synthetase cDNA. In testis, an FPP synthetase-related RNA was detected that was larger than the liver FPP synthetase mRNA and was present at very high levels comparable with liver FPP synthetase RNA levels obtained from rats fed diets supplemented with cholestyramine and mevinolin. Sequence analysis of testis cDNA clones, together with primer extension and S1 nuclease experiments, indicated that testis FPP synthetase transcripts contain an extended 5' untranslated region. The 5' extension contained one or two out-of-frame upstream ATGs, depending on the site of transcription initiation. Protein in vitro translation studies indicated that the extended 5' untranslated region may play a role in regulating the translation of the FPP synthetase polypeptide in rat testis. Southern blot analysis with a probe containing both testis and liver 5' untranslated sequences provided evidence that both liver and testis transcripts derive from the same gene. The data suggest that an upstream testis-specific promoter results in the abundant production of FPP synthetase transcripts that are translated at low efficiency; another promoter functions in liver and other somatic tissues and directs the regulated synthesis of shorter discrete transcripts.

scholarly journals Prostaglandin E1 inhibits endocytosis in the β-cell endocytosis

2016 ◽  
Vol 229 (3) ◽  
pp. 287-294 ◽  
Author(s):  
Ying Zhao ◽  
Qinghua Fang ◽  
Susanne G Straub ◽  
Manfred Lindau ◽  
Geoffrey W G Sharp
Keyword(s):  
Inhibitory Effect ◽  
Prostaglandin E ◽  
Β Cell ◽  
Α Subunit ◽  
Capacitance Measurements ◽  
Readily Releasable Pool ◽  
Whole Cell Patch Clamp ◽  
C Terminus ◽  
High Level

Prostaglandins inhibit insulin secretion in a manner similar to that of norepinephrine (NE) and somatostatin. As NE inhibits endocytosis as well as exocytosis, we have now examined the modulation of endocytosis by prostaglandin E1 (PGE1). Endocytosis following exocytosis was recorded by whole-cell patch clamp capacitance measurements in INS-832/13 cells. Prolonged depolarizing pulses producing a high level of Ca2+ influx were used to stimulate maximal exocytosis and to deplete the readily releasable pool (RRP) of granules. This high Ca2+ influx eliminates the inhibitory effect of PGE1 on exocytosis and allows specific characterization of the inhibitory effect of PGE1 on the subsequent compensatory endocytosis. After stimulating exocytosis, endocytosis was apparent under control conditions but was inhibited by PGE1 in a Pertussis toxin-sensitive (PTX)-insensitive manner. Dialyzing a synthetic peptide mimicking the C-terminus of the α-subunit of the heterotrimeric G-protein Gz into the cells blocked the inhibition of endocytosis by PGE1, whereas a control-randomized peptide was without effect. These results demonstrate that PGE1 inhibits endocytosis and Gz mediates the inhibition.

Expression of the G-protein α-subunit gustducin in mammalian spermatozoa

2006 ◽  
Vol 193 (1) ◽  
pp. 21-34 ◽  
Author(s):  
Johanna Fehr ◽  
Dorke Meyer ◽  
Patricia Widmayer ◽  
Heike Claudia Borth ◽  
Frauke Ackermann ◽  
...  
Keyword(s):  
G Protein ◽  
Α Subunit ◽  
G Protein Α Subunit ◽  
Mammalian Spermatozoa

Development of a novel transgenic rice with hypocholesterolemic activity via high-level accumulation of the α′ subunit of soybean β-conglycinin

2014 ◽  
Vol 23 (4) ◽  
pp. 609-620 ◽  
Author(s):  
Cerrone Cabanos ◽  
Naoki Kato ◽  
Yoshiki Amari ◽  
Keigo Fujiwara ◽  
Tomoki Ohno ◽  
...  
Keyword(s):  
Transgenic Rice ◽  
Α Subunit ◽  
High Level

scholarly journals Expression of a novel reticulon-like gene in human testis

Reproduction ◽  
2002 ◽  
pp. 227-234 ◽  
Author(s):  
ZM Zhou ◽  
JH Sha ◽  
JM Li ◽  
M Lin ◽  
H Zhu ◽  
...  
Keyword(s):  
Short Form ◽  
Expression Profiles ◽  
Differentially Expressed ◽  
Human Testis ◽  
Nylon Membrane ◽  
Adult Testis ◽  
Fetal Testis ◽  
Pcr Products ◽  
Testis Cdna ◽  
Membrane Spanning

Identification of genes that are specifically expressed in the adult testis or the fetal testis is important for the study of genes related to the development of the testis. In this study, a human testis cDNA microarray was established. PCR products of 9216 clones from a human testis cDNA library were dotted on a nylon membrane; mRNA from adult and fetal testes were purified and probes were prepared by a reverse transcription reaction with testis mRNA as template. The microarray was hybridized with probes of adult and fetal testes, and 96.8 and 95.4% of clones were positive, respectively. In total, 731 clones were differentially expressed: 592 were highly expressed in adult testis and 139 were highly expressed in fetal testis. Among these genes, a new reticulon (Rtn)-like gene was detected and named Rtn-T. Rtn-T was highly expressed in adult human testis. The cDNA of Rtn-T contains 3491 bp and the putative protein had 968 amino acids. This protein is homologous to the six known members of the Rtn family (KIAA0886, Rtn xL, reticulon 4a, Nogo-A, Nogo-A short form, and brain my043) but was different at the 5' end. All homologues originate from one gene, and result from both different promotor regions and different splicing. Rtn-T lacks the first exon and contains a second exon that is lacking in the other homologues. Rtn-T is shorter than KIAA0886, Rtn xL, reticulon 4a and Nogo-A, but longer than the Nogo-A short form and brain my043. Sequence analysis showed that Rtn-T protein has two hydrophobic regions that may be membrane-spanning domains. Expression profiles showed that Rtn-T is specifically and strongly expressed in testis. The results of the present study indicate that the Rtn-T gene is differentially expressed in adult and fetal testes and encodes a membrane protein that may have a function in testis development.

scholarly journals Cell-Specific Expression of the Mouse Glycoprotein Hormone α-Subunit Gene Requires Multiple Interacting DNA Elements in Transgenic Mice and Cultured Cells

1998 ◽  
Vol 12 (5) ◽  
pp. 622-633 ◽  
Author(s):  
Michelle L. Brinkmeier ◽  
David F. Gordon ◽  
Janet M. Dowding ◽  
Thomas L. Saunders ◽  
Susan K. Kendall ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Pituitary Cells ◽  
Subunit Gene ◽  
High Level Expression ◽  
Glycoprotein Hormone ◽  
Α Subunit ◽  
Peripheral Tissues ◽  
Cell Specificity ◽  
Dna Elements ◽  
High Level

Abstract The glycoprotein hormone α-subunit gene is expressed and differentially regulated in pituitary gonadotropes and thyrotropes. Previous gene expression studies suggested that cell specificity may be regulated by distinct DNA elements. We have identified an enhancer region between −4.6 and −3.7 kb that is critical for high level expression in both gonadotrope and thyrotrope cells of transgenic mice. Fusion of the enhancer to −341/+43 mouseα -subunit promoter results in appropriate pituitary cell specificity and transgene expression levels that are similar to levels observed with the intact −4.6 kb/+43 construct. Deletion of sequences between− 341 and −297 resulted in a loss of high level expression and cell specificity, exhibited by ectopic transgene activation in GH-, ACTH-, and PRL-producing pituitary cells as well as in other peripheral tissues. Consistent with these results, transient cell transfection studies demonstrated that the enhancer stimulated activity of a− 341/+43 α-promoter in both αTSH and αT3 cells, but it did not enhance α-promoter activity significantly in CV-1 cells. Removal of sequences between −341 and −297 allowed the enhancer to function in heterologous cells. Loss of high level expression and cell specificity may be due to loss of sequences required for binding of the LIM homeoproteins or the α-basal element 1. These data demonstrate that the enhancer requires participation by both proximal and distal sequences for high level expression and suggests that sequences from− 341 to −297 are critical for restricting expression to the anterior pituitary.

Sign in / Sign up

Export Citation Format

Share Document